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Conserved domains on  [gi|1466031370|gb|RGE15779|]
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exodeoxyribonuclease III [Desulfotomaculum sp. OF05-3]

Protein Classification

exodeoxyribonuclease III( domain architecture ID 10173395)

exodeoxyribonuclease III is a Mg-dependent 3' to 5' exonuclease acting on dsDNA, which releases 5' phosphomononucleotides as degradation products; similar to bacterial exodeoxyribonuclease III and eukaryotic DNA-(apurinic or apyrimidinic site) endonuclease

CATH:  3.60.10.10
EC:  3.1.11.2
Gene Ontology:  GO:0003677|GO:0046872|GO:0004519|GO:0004527|GO:0006281|GO:0008311
PubMed:  7885481|10838565
SCOP:  4002213

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 3-250 8.05e-176

Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This subfamily includes human Ape1 (also known as Apex, Hap1, or Ref-1) and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Ape1 and Ape2 in humans. Ape1 is found in this subfamily, it exhibits strong AP-endonuclease activity but shows weak 3'-5' exonuclease and 3'-phosphodiesterase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


:

Pssm-ID: 197321 [Multi-domain]  Cd Length: 253  Bit Score: 483.59  E-value: 8.05e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQVELE----LPGYHQYWNYAEKKGYSGTAMFTKEEPIAVT 78
Cdd:cd09087     2 KIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  79 YGLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNP 158
Cdd:cd09087    82 YGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLANP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 159 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 238
Cdd:cd09087   162 KTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSDI 241

                         250
                  ....*....|..
gi 1466031370 239 MGSDHCPVELDI 250
Cdd:cd09087   242 MGSDHCPIGLEL 253
 
Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 3-250 8.05e-176

Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This subfamily includes human Ape1 (also known as Apex, Hap1, or Ref-1) and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Ape1 and Ape2 in humans. Ape1 is found in this subfamily, it exhibits strong AP-endonuclease activity but shows weak 3'-5' exonuclease and 3'-phosphodiesterase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197321 [Multi-domain]  Cd Length: 253  Bit Score: 483.59  E-value: 8.05e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQVELE----LPGYHQYWNYAEKKGYSGTAMFTKEEPIAVT 78
Cdd:cd09087     2 KIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  79 YGLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNP 158
Cdd:cd09087    82 YGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLANP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 159 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 238
Cdd:cd09087   162 KTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSDI 241

                         250
                  ....*....|..
gi 1466031370 239 MGSDHCPVELDI 250
Cdd:cd09087   242 MGSDHCPIGLEL 253
XthA COG0708
Exonuclease III [Replication, recombination and repair];
3-250 2.70e-141

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 396.37  E-value: 2.70e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKgFLEYVKESDVDIFCIQESKCQEGQV---ELELPGYHQYWNYaeKKGYSGTAMFTKEEPIAVTY 79
Cdd:COG0708     2 KIASWNVNGIRARLPK-LLDWLAEEDPDVLCLQETKAQDEQFpleAFEAAGYHVYFHG--QKGYNGVAILSRLPPEDVRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQD-GLKRLDYRMQWEDAFRAYLKEL-ETKKPVIFCGDLNVAHQEIDLKN 157
Cdd:COG0708    79 GLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSvGSEKFDYKLRFLDALRAYLAELlAPGRPLILCGDFNIAPTEIDVKN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 158 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 237
Cdd:COG0708   159 PKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDRE 238

                         250
                  ....*....|....*..
gi 1466031370 238 ----VMGSDHCPVELDI 250
Cdd:COG0708   239 prgdERPSDHAPVVVEL 255
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 3-250 2.76e-137

exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are 5' AP endonucleases that funciton in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273186 [Multi-domain]  Cd Length: 254  Bit Score: 386.25  E-value: 2.76e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQ---VELELPGYHQYWNYAeKKGYSGTAMFTKEEPIAVTY 79
Cdd:TIGR00633   2 KIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQfpaELFEELGYHVFFHGA-KKGYSGVAILSKVEPLDVRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQ-DGLKRLDYRMQ-WEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKN 157
Cdd:TIGR00633  81 GFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGsRDLERLEYKLQfWDALFQYLEKELDAGKPVVICGDMNVAHTEIDLGN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 158 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 237
Cdd:TIGR00633 161 PKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYIDSE 240

                         250
                  ....*....|...
gi 1466031370 238 VMGSDHCPVELDI 250
Cdd:TIGR00633 241 IRGSDHCPIVLEL 253
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
 3-250 2.21e-122

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 348.22  E-value: 2.21e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQVELELPGYHQYWNYAEKKGYSGTAMFTKEEPIAVTYGLG 82
Cdd:PRK13911    2 KLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQNTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSYGIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  83 IEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNPKTNR 162
Cdd:PRK13911   82 IEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENPKTNR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 163 KNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEVMGSD 242
Cdd:PRK13911  162 KNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDILGSD 241


                  ....*...
gi 1466031370 243 HCPVELDI 250
Cdd:PRK13911  242 HCPVGLEL 249
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 5-148 9.82e-19

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 81.12  E-value: 9.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   5 ISWNVNGLRA------CLGKGFLEYVKESDVDIFCIQESKCQEGQV----ELELPGYHQYWNYAEKKGYSGTAMFTKEEP 74
Cdd:pfam03372   1 LTWNVNGGNAdaagddRKLDALAALIRAYDPDVVALQETDDDDASRlllaLLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466031370  75 IAVTYGLGIEEHDHEGRVITAEFPEYYVV-TCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNV 148
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVpLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
 
Name Accession Description Interval E-value
Ape1-like_AP-endo cd09087
Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This ...
 3-250 8.05e-176

Human Ape1-like subfamily of the ExoIII family apurinic/apyrimidinic (AP) endonucleases; This subfamily includes human Ape1 (also known as Apex, Hap1, or Ref-1) and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Ape1 and Ape2 in humans. Ape1 is found in this subfamily, it exhibits strong AP-endonuclease activity but shows weak 3'-5' exonuclease and 3'-phosphodiesterase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197321 [Multi-domain]  Cd Length: 253  Bit Score: 483.59  E-value: 8.05e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQVELE----LPGYHQYWNYAEKKGYSGTAMFTKEEPIAVT 78
Cdd:cd09087     2 KIISWNVNGLRALLKKGLLDYVKKEDPDILCLQETKLQEGDVPKElkelLKGYHQYWNAAEKKGYSGTAILSKKKPLSVT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  79 YGLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNP 158
Cdd:cd09087    82 YGIGIEEHDQEGRVITAEFENFYLVNTYVPNSGRGLERLDRRKEWDVDFRAYLKKLDSKKPVIWCGDLNVAHEEIDLANP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 159 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 238
Cdd:cd09087   162 KTNKKSAGFTPEERESFTELLEAGFVDTFRHLHPDKEGAYTFWSYRGNARAKNVGWRLDYFLVSERLKDRVVDSFIRSDI 241

                         250
                  ....*....|..
gi 1466031370 239 MGSDHCPVELDI 250
Cdd:cd09087   242 MGSDHCPIGLEL 253
XthA COG0708
Exonuclease III [Replication, recombination and repair];
3-250 2.70e-141

Exonuclease III [Replication, recombination and repair];


Pssm-ID: 440472 [Multi-domain]  Cd Length: 256  Bit Score: 396.37  E-value: 2.70e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKgFLEYVKESDVDIFCIQESKCQEGQV---ELELPGYHQYWNYaeKKGYSGTAMFTKEEPIAVTY 79
Cdd:COG0708     2 KIASWNVNGIRARLPK-LLDWLAEEDPDVLCLQETKAQDEQFpleAFEAAGYHVYFHG--QKGYNGVAILSRLPPEDVRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQD-GLKRLDYRMQWEDAFRAYLKEL-ETKKPVIFCGDLNVAHQEIDLKN 157
Cdd:COG0708    79 GLGGDEFDAEGRYIEADFGGVRVVSLYVPNGGSvGSEKFDYKLRFLDALRAYLAELlAPGRPLILCGDFNIAPTEIDVKN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 158 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 237
Cdd:COG0708   159 PKANLKNAGFLPEERAWFDRLLELGLVDAFRALHPDVEGQYTWWSYRAGAFARNRGWRIDYILASPALADRLKDAGIDRE 238

                         250
                  ....*....|....*..
gi 1466031370 238 ----VMGSDHCPVELDI 250
Cdd:COG0708   239 prgdERPSDHAPVVVEL 255
xth TIGR00633
exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are ...
 3-250 2.76e-137

exodeoxyribonuclease III (xth); All proteins in this family for which functions are known are 5' AP endonucleases that funciton in base excision repair and the repair of abasic sites in DNA.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273186 [Multi-domain]  Cd Length: 254  Bit Score: 386.25  E-value: 2.76e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQ---VELELPGYHQYWNYAeKKGYSGTAMFTKEEPIAVTY 79
Cdd:TIGR00633   2 KIISWNVNGLRARLHKLFLDWLKEEQPDVLCLQETKVADEQfpaELFEELGYHVFFHGA-KKGYSGVAILSKVEPLDVRY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQ-DGLKRLDYRMQ-WEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKN 157
Cdd:TIGR00633  81 GFGGEPHDEEGRVITAEFDGFTVVNVYVPNGGsRDLERLEYKLQfWDALFQYLEKELDAGKPVVICGDMNVAHTEIDLGN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 158 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 237
Cdd:TIGR00633 161 PKENKGNAGFTPEEREWFDELLEAGFVDTFRHFNPDTGDAYTWWDYRSGARDRNRGWRIDYFLVSEPLAERVVDSYIDSE 240

                         250
                  ....*....|...
gi 1466031370 238 VMGSDHCPVELDI 250
Cdd:TIGR00633 241 IRGSDHCPIVLEL 253
ExoIII_AP-endo cd09073
Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ...
 3-248 3.02e-133

Escherichia coli exonuclease III (ExoIII)-like apurinic/apyrimidinic (AP) endonucleases; The ExoIII family AP endonucleases belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, which is then followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, which have both mutagenic and cytotoxic effects. AP endonucleases can carry out a wide range of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two functional AP endonucleases, for example, APE1/Ref-1 and Ape2 in humans, Apn1 and Apn2 in bakers yeast, Nape and NExo in Neisseria meningitides, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. Usually, one of the two is the dominant AP endonuclease, the other has weak AP endonuclease activity, but exhibits strong 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, and 3'-phosphatase activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes. This family contains the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197307 [Multi-domain]  Cd Length: 251  Bit Score: 375.86  E-value: 3.02e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQVELEL---PGYHQYWNYAEKKGYSGTAMFTKEEPIAVTY 79
Cdd:cd09073     1 KIISWNVNGLRARLKKGVLKWLKEEKPDILCLQETKADEDKLPEELqhvEGYHSYWSPARKKGYSGVATLSKEEPLDVSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETK-KPVIFCGDLNVAHQEIDLKNP 158
Cdd:cd09073    81 GIGGEEFDSEGRVITAEFDDFYLINVYFPNGGRGLERLDYKLRFYEAFLEFLEKLRKRgKPVVICGDFNVAHEEIDLARP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 159 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDqEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 238
Cdd:cd09073   161 KKNEKNAGFTPEERAWFDKLLSLGYVDTFRHFHPE-PGAYTWWSYRGNARERNVGWRIDYFLVSEELAEKVKDSGILSKV 239

                         250
                  ....*....|
gi 1466031370 239 MGSDHCPVEL 248
Cdd:cd09073   240 KGSDHAPVTL 249
Mth212-like_AP-endo cd09085
Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic ...
 3-250 7.73e-133

Methanothermobacter thermautotrophicus Mth212-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes the thermophilic archaeon Methanothermobacter thermautotrophicus Mth212and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Mth212 is an AP endonuclease, and a DNA uridine endonuclease (U-endo) that nicks double-stranded DNA at the 5'-side of a 2'-d-uridine residue. After incision at the 5'-side of a 2'-d-uridine residue by Mth212, DNA polymerase B takes over the 3'-OH terminus and carries out repair synthesis, generating a 5'-flap structure that is resolved by a 5'-flap endonuclease. Finally, DNA ligase seals the resulting nick. This U-endo activity shares the same catalytic center as its AP-endo activity, and is absent from other AP endonuclease homologues.


Pssm-ID: 197319 [Multi-domain]  Cd Length: 252  Bit Score: 374.69  E-value: 7.73e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQVELEL---PGYHQYWNYAEKKGYSGTAMFTKEEPIAVTY 79
Cdd:cd09085     2 KIISWNVNGLRAVHKKGFLDWFKEEKPDILCLQETKAQPEQLPEDLrniEGYHSYFNSAERKGYSGVALYSKIEPDSVRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETK-KPVIFCGDLNVAHQEIDLKNP 158
Cdd:cd09085    82 GLGVEEFDNEGRILIADFDDFTLFNIYFPNGQMSEERLDYKLEFYDAFLEYLNELRDSgKNVIICGDFNTAHKEIDLARP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 159 KTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDqEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEV 238
Cdd:cd09085   162 KENEKVSGFLPEERAWMDKFIENGYVDTFRMFNKE-PGQYTWWSYRTRARERNVGWRIDYFFVNEEFKPKVKDAGILPDV 240

                         250
                  ....*....|..
gi 1466031370 239 MGSDHCPVELDI 250
Cdd:cd09085   241 MGSDHCPVSLEL 252
exoDNase_III TIGR00195
exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model ...
 3-250 1.27e-122

exodeoxyribonuclease III; The model brings in reverse transcriptases at scores below 50, model also contains eukaryotic apurinic/apyrimidinic endonucleases which group in the same family [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 272954 [Multi-domain]  Cd Length: 254  Bit Score: 348.99  E-value: 1.27e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGfLEYVKESDVDIFCIQESKCQEGQVELELP---GYHQYWNYAekKGYSGTAMFTKEEPIAVTY 79
Cdd:TIGR00195   2 KIISWNVNGLRARPHKG-LAWLKENQPDVLCLQETKVQDEQFPLEPFhkeGYHVFFSGQ--KGYSGVAIFSKEEPISVRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPN-SQDGLKRLDYRMQWEDAFRAYLKELETK-KPVIFCGDLNVAHQEIDLKN 157
Cdd:TIGR00195  79 GFGVEEEDAEGRIIMAEFDSFLVINGYFPNgSRDDSEKLPYKLQWLEALQNYLEKLVDKdKPVLICGDMNIAPTEIDLHI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 158 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDqEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 237
Cdd:TIGR00195 159 PDENRNHTGFLPEEREWLDRLLEAGLVDTFRKFNPD-EGAYSWWDYRTKARDRNRGWRIDYFLVSEPLKERCVDCGIDYD 237

                         250
                  ....*....|....*..
gi 1466031370 238 VMG----SDHCPVELDI 250
Cdd:TIGR00195 238 IRGsekpSDHCPVVLEF 254
PRK13911 PRK13911
exodeoxyribonuclease III; Provisional
 3-250 2.21e-122

exodeoxyribonuclease III; Provisional


Pssm-ID: 139971 [Multi-domain]  Cd Length: 250  Bit Score: 348.22  E-value: 2.21e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQVELELPGYHQYWNYAEKKGYSGTAMFTKEEPIAVTYGLG 82
Cdd:PRK13911    2 KLISWNVNGLRACMTKGFMDFFNSVDADVFCIQESKMQQEQNTFEFKGYFDFWNCAIKKGYSGVVTFTKKEPLSVSYGIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  83 IEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQEIDLKNPKTNR 162
Cdd:PRK13911   82 IEEHDKEGRVITCEFESFYLVNVYTPNSQQALSRLSYRMSWEVEFKKFLKALELKKPVIVCGDLNVAHNEIDLENPKTNR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 163 KNAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEVMGSD 242
Cdd:PRK13911  162 KNAGFSDEERGKFSELLNAGFIDTFRYFYPNKEKAYTWWSYMQQARDKNIGWRIDYFLCSNPLKTRLKDALIYKDILGSD 241


                  ....*...
gi 1466031370 243 HCPVELDI 250
Cdd:PRK13911  242 HCPVGLEL 249
Nape_like_AP-endo cd10281
Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) ...
 3-250 4.03e-104

Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes Neisseria meningitides Nape and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Neisseria meningitides Nape and NExo. Nape, found in this subfamily, is the dominant AP endonuclease. It exhibits strong AP endonuclease activity, and also exhibits 3'-5'exonuclease and 3'-deoxyribose phosphodiesterase activities.


Pssm-ID: 197336 [Multi-domain]  Cd Length: 253  Bit Score: 302.22  E-value: 4.03e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKGFLEYVKESDVDIFCIQESKCQEGQVE---LELPGYHQYWNYAEKKGYSGTAMFTKEEPIAVTY 79
Cdd:cd10281     2 RVISVNVNGIRAAAKKGFLEWLAAQDADVVCLQEVRAQEEQLDddfFEPEGYNAYFFDAEKKGYAGVAIYSRTQPKAVIY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKP-VIFCGDLNVAHQEIDLKNP 158
Cdd:cd10281    82 GLGFEEFDDEGRYIEADFDNVSVASLYVPSGSSGDERQEAKMAFLDAFLEHLKELRRKRReFIVCGDFNIAHTEIDIKNW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 159 KTNRKNAGFSDEERAKFTELL-EAGFVDTFRYFYPDQeGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 237
Cdd:cd10281   162 KANQKNSGFLPEERAWLDQVFgELGYVDAFRELNPDE-GQYTWWSNRGQARANNVGWRIDYQIATPGLASKVVSAWIYRE 240

                         250
                  ....*....|...
gi 1466031370 238 VMGSDHCPVELDI 250
Cdd:cd10281   241 ERFSDHAPLIVDY 253
ExoIII-like_AP-endo cd09086
Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of ...
 3-246 8.37e-81

Escherichia coli exonuclease III (ExoIII) and Neisseria meningitides NExo-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes Escherichia coli ExoIII, Neisseria meningitides NExo,and related proteins. These are ExoIII family AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiencies. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For example, Neisseria meningitides Nape and NExo, and exonuclease III (ExoIII) and endonuclease IV (EndoIV) in Escherichia coli. NExo and ExoIII are found in this subfamily. NExo is the non-dominant AP endonuclease. It exhibits strong 3'-5' exonuclease and 3'-deoxyribose phosphodiesterase activities. Escherichia coli ExoIII is an active AP endonuclease, and in addition, it exhibits double strand (ds)-specific 3'-5' exonuclease, exonucleolytic RNase H, 3'-phosphomonoesterase and 3'-phosphodiesterase activities, all catalyzed by a single active site. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes ExoIII and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197320 [Multi-domain]  Cd Length: 254  Bit Score: 242.81  E-value: 8.37e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKgFLEYVKESDVDIFCIQESKCQEGQ---VELELPGYHQYWNyaEKKGYSGTAMFTKEEPIAVTY 79
Cdd:cd09086     2 KIATWNVNSIRARLEQ-VLDWLKEEDPDVLCLQETKVEDDQfpaDAFEALGYHVAVH--GQKAYNGVAILSRLPLEDVRT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  80 GLGIEEHDHEGRVITAEFPEYYVVTCYTPNSQD-GLKRLDYRMQWEDAFRAYL-KELETKKPVIFCGDLNVAHQEIDLKN 157
Cdd:cd09086    79 GFPGDPDDDQARLIAARVGGVRVINLYVPNGGDiGSPKFAYKLDWLDRLIRYLqKLLKPDDPLVLVGDFNIAPEDIDVWD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 158 PKTNRKNAGFSDEERAKFTELLEAGFVDTFRYFYPDqEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTE 237
Cdd:cd09086   159 PKQLLGKVLFTPEEREALRALLDLGFVDAFRALHPD-EKLFTWWDYRAGAFERNRGLRIDHILASPALADRLKDVGIDRE 237

                         250
                  ....*....|...
gi 1466031370 238 VMG----SDHCPV 246
Cdd:cd09086   238 PRGwekpSDHAPV 250
Ape2-like_AP-endo cd09088
Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This ...
 3-250 4.24e-52

Human Ape2-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases; This subfamily includes human APE2, Saccharomyces cerevisiae Apn2/Eth1, and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and they belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER, the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity. For examples, Ape1 and Ape2 in humans, and Apn1 and Apn2 in bakers yeast. Ape2 and Apn2/Eth1 are both found in this subfamily, and have the weaker AP endonuclease activity. Ape2 shows strong 3'-5' exonuclease and 3'-phosphodiesterase activities; it can reduce the mutagenic consequences of attack by reactive oxygen species by removing 3'-end adenine opposite from 8-oxoG, in addition to repairing 3'-damaged termini. Apn2/Eth1 exhibits AP endonuclease activity, but has 30-40 fold more active 3'-phosphodiesterase and 3'-5' exonuclease activities. Class II AP endonucleases have been classified into two families, designated ExoIII and EndoIV, based on their homology to the Escherichia coli enzymes exonuclease III (ExoIII) and endonuclease IV (EndoIV). This subfamily belongs to the ExoIII family; the EndoIV family belongs to a different superfamily.


Pssm-ID: 197322 [Multi-domain]  Cd Length: 309  Bit Score: 171.35  E-value: 4.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLG-------KGFLEYVKESDVDIFCIQESKCQEGQVELE---LPGYHQYWNY-AEKKGYSGTAMFTK 71
Cdd:cd09088     1 RIVTWNVNGIRTRLQyqpwnkeNSLKSFLDSLDADIICLQETKLTRDELDEPsaiVEGYDSFFSFsRGRKGYSGVATYCR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  72 ---EEPIAVTYGL-----------GIEEH---------------------DHEGRVITAEFPEYYVVTCYTP-NSQDGLK 115
Cdd:cd09088    81 dsaATPVAAEEGLtgvlsspnqknELSENddigcygemleftdskellelDSEGRCVLTDHGTFVLINVYCPrADPEKEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 116 RLDYRMqwedAFRAYLKE-----LETKKPVIFCGDLNVAHQEIDLKNPKTNRKNAGFSDEE---RAKFTELLEAG----- 182
Cdd:cd09088   161 RLEFKL----DFYRLLEErvealLKAGRRVILVGDVNVSHRPIDHCDPDDSEDFGGESFEDnpsRQWLDQLLGDSgeggg 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1466031370 183 -----FVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESLKDRLVDAKIHTEVMGSDHCPVELDI 250
Cdd:cd09088   237 spgglLIDSFRYFHPTRKGAYTCWNTLTGARPTNYGTRIDYILADRGLLPWVKAADILPEVEGSDHCPVYADL 309
PRK11756 PRK11756
exonuclease III; Provisional
 3-250 1.53e-42

exonuclease III; Provisional


Pssm-ID: 236970 [Multi-domain]  Cd Length: 268  Bit Score: 145.42  E-value: 1.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKgfLEYVKES-DVDIFCIQESKCQEGQVELELP---GYHQYwnYAEKKGYSGTAMFTKEEPIAVT 78
Cdd:PRK11756    2 KFVSFNINGLRARPHQ--LEAIIEKhQPDVIGLQETKVHDEMFPLEEVealGYHVF--YHGQKGHYGVALLSKQTPIAVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  79 YGLGIEEHDHEGRVITAEFP----EYYVVTCYTPN--SQDGLKRLDYRMQWEDAFRAYLKELETK-KPVIFCGDLNVAHQ 151
Cdd:PRK11756   78 KGFPTDDEEAQRRIIMATIPtpngNLTVINGYFPQgeSRDHPTKFPAKRQFYQDLQNYLETELSPdNPLLIMGDMNISPT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 152 EIDLKNPKTNRK------NAGFSDEERAKFTELLEAGFVDTFRYFYPDQEGIYSWWSYRFSARAKNAGWRIDYFCVSESL 225
Cdd:PRK11756  158 DLDIGIGEENRKrwlrtgKCSFLPEEREWLDRLMDWGLVDTFRQLNPDVNDRFSWFDYRSKGFDDNRGLRIDLILATQPL 237

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1466031370 226 KDRLVDAKIHTEVMG----SDHCPV--ELDI 250
Cdd:PRK11756  238 AERCVETGIDYDIRGmekpSDHAPIwaTFKL 268
EEP cd08372
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes ...
 5-250 3.21e-37

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.


Pssm-ID: 197306 [Multi-domain]  Cd Length: 241  Bit Score: 131.06  E-value: 3.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   5 ISWNVNGLRAC-LGKGFLEYVKESDVDIFCIQESKC-QEGQVELELPGYHQYWNYA----EKKGYSGTAMFTK---EEPI 75
Cdd:cd08372     2 ASYNVNGLNAAtRASGIARWVRELDPDIVCLQEVKDsQYSAVALNQLLPEGYHQYQsgpsRKEGYEGVAILSKtpkFKIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  76 AVTYGLGIEEHDHEGRVITAEF----PEYYVVTCYTPNsqdGLKRLDYRMQWEDAFRAYLKELETKK--PVIFCGDLNVA 149
Cdd:cd08372    82 EKHQYKFGEGDSGERRAVVVKFdvhdKELCVVNAHLQA---GGTRADVRDAQLKEVLEFLKRLRQPNsaPVVICGDFNVR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 150 HQEIDLKNPKtnrknagfsdeerAKFTELLEAGFVDTfryfYPDQEGIYSWWSYRfsaraKNAGWRIDYFCVSESLKDRL 229
Cdd:cd08372   159 PSEVDSENPS-------------SMLRLFVALNLVDS----FETLPHAYTFDTYM-----HNVKSRLDYIFVSKSLLPSV 216

                         250       260
                  ....*....|....*....|....*
gi 1466031370 230 VDAKIHTEV----MGSDHCPVELDI 250
Cdd:cd08372   217 KSSKILSDAararIPSDHYPIEVTL 241
L1-EN cd09076
Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; ...
 5-250 2.32e-26

Endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains; This family contains the endonuclease domain (L1-EN) of the non-LTR retrotransposon LINE-1 (L1), and related domains, including the endonuclease of Xenopus laevis Tx1. These retrotranspons belong to the subtype 2, L1-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. LINE-1/L1 elements (full length and truncated) comprise about 17% of the human genome. This endonuclease nicks the genomic DNA at the consensus target sequence 5'TTTT-AA3' producing a ribose 3'-hydroxyl end as a primer for reverse transcription of associated template RNA. This subgroup also includes the endonuclease of Xenopus laevis Tx1, another member of the L1-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197310 [Multi-domain]  Cd Length: 236  Bit Score: 102.43  E-value: 2.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   5 ISWNVNGL-----RACLgkgfLEYVKESDVDIFCIQESKC-QEGQVELELPGYHQYWNYAEKKGYSGTA-MFTKE-EPIA 76
Cdd:cd09076     2 GTLNVRGLrspgkRAQL----LEELKRKKLDILGLQETHWtGEGELKKKREGGTILYSGSDSGKSRGVAiLLSKTaANKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  77 VTYglgieEHDHEGRVITAEF----PEYYVVTCYTPNSQDGlkrlDYRMQWEDAFRAYLKELETKKPVIFCGDLNVAHQE 152
Cdd:cd09076    78 LEY-----TKVVSGRIIMVRFkikgKRLTIINVYAPTARDE----EEKEEFYDQLQDVLDKVPRHDTLIIGGDFNAVLGP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 153 IDLKNPKTNRKNagfSDEERAKFTELLEAGFVDTFRYFYPDQEGiYSWWSYRFSARAknagwRIDYFCVSESLKDRLVDA 232
Cdd:cd09076   149 KDDGRKGLDKRN---ENGERALSALIEEHDLVDVWRENNPKTRE-YTWRSPDHGSRS-----RIDRILVSKRLRVKVKKT 219

                         250
                  ....*....|....*...
gi 1466031370 233 KIhTEVMGSDHCPVELDI 250
Cdd:cd09076   220 KI-TPGAGSDHRLVTLKL 236
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 5-148 9.82e-19

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 81.12  E-value: 9.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   5 ISWNVNGLRA------CLGKGFLEYVKESDVDIFCIQESKCQEGQV----ELELPGYHQYWNYAEKKGYSGTAMFTKEEP 74
Cdd:pfam03372   1 LTWNVNGGNAdaagddRKLDALAALIRAYDPDVVALQETDDDDASRlllaLLAYGGFLSYGGPGGGGGGGGVAILSRYPL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1466031370  75 IAVTYGLGIEEHDHEGRVITAEFPEYYVV-TCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKKPVIFCGDLNV 148
Cdd:pfam03372  81 SSVILVDLGEFGDPALRGAIAPFAGVLVVpLVLTLAPHASPRLARDEQRADLLLLLLALLAPRSEPVILAGDFNA 155
EEP-2 cd09084
Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This ...
 4-250 3.02e-11

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily; uncharacterized family 2; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps, proteins.


Pssm-ID: 197318 [Multi-domain]  Cd Length: 246  Bit Score: 61.54  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   4 MISWNVNGLRAC----LGKGFLEYVKESDVDIFCIQESKCQEGQ----VELELPGY-HQYWNYAEKKGYSGTAMFTKeEP 74
Cdd:cd09084     1 VMSYNVRSFNRYkwkdDPDKILDFIKKQDPDILCLQEYYGSEGDkdddLRLLLKGYpYYYVVYKSDSGGTGLAIFSK-YP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  75 I----AVTYGLGIE-----EHDHEGRVIT-------------AEFPEYYVVTCYTPNSQDGLKRLDYRMQWE----DAFR 128
Cdd:cd09084    80 IlnsgSIDFPNTNNnaifaDIRVGGDTIRvynvhlesfritpSDKELYKEEKKAKELSRNLLRKLAEAFKRRaaqaDLLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 129 AYLKelETKKPVIFCGDLNvahqeidlknpktnrkNAGFSDEERakfteLLEAGFVDTFRyfypdqegiYSWWSYRFSAR 208
Cdd:cd09084   160 ADIA--ASPYPVIVCGDFN----------------DTPASYVYR-----TLKKGLTDAFV---------EAGSGFGYTFN 207

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1466031370 209 AKNAGWRIDYFCVSESLkdRLVDAKIHTEVMgSDHCPVELDI 250
Cdd:cd09084   208 GLFFPLRIDYILTSKGF--KVLRYRVDPGKY-SDHYPIVATL 246
YafD COG3021
Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily ...
 3-246 6.39e-07

Uncharacterized conserved protein YafD, endonuclease/exonuclease/phosphatase (EEP) superfamily [General function prediction only];


Pssm-ID: 442257 [Multi-domain]  Cd Length: 310  Bit Score: 49.22  E-value: 6.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   3 KMISWNVNGLRACLGKgFLEYVKESDVDIFCIQESKcQEGQVELE-LPGYHQYWNYAEKKGYSGTAMFTKEEPIAVTygl 81
Cdd:COG3021    96 RVLTANVLFGNADAEA-LAALVREEDPDVLVLQETT-PAWEEALAaLEADYPYRVLCPLDNAYGMALLSRLPLTEAE--- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  82 GIEEHDHEGRVITAEF------PEYYVVTCYTPnsqdglkrLDYRMQWEDAFRAYLKEL-ETKKPVIFCGDLN-VAHQei 153
Cdd:COG3021   171 VVYLVGDDIPSIRATVelpggpVRLVAVHPAPP--------VGGSAERDAELAALAKAVaALDGPVIVAGDFNaTPWS-- 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 154 dlknPKTNR--KNAGFSDEERAkftelleAGFVDTFRYFYPdqegiyswwsyrfsarakNAGWRIDYFCVSESLkdRLVD 231
Cdd:COG3021   241 ----PTLRRllRASGLRDARAG-------RGLGPTWPANLP------------------FLRLPIDHVLVSRGL--TVVD 289

                         250
                  ....*....|....*
gi 1466031370 232 AKIHtEVMGSDHCPV 246
Cdd:COG3021   290 VRVL-PVIGSDHRPL 303
R1-I-EN cd09077
Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat ...
 7-250 4.39e-05

Endonuclease domain encoded by various R1- and I-clade non-long terminal repeat retrotransposons; This family contains the endonuclease (EN) domain of various non-long terminal repeat (non-LTR) retrotransposons, long interspersed nuclear elements (LINEs) which belong to the subtype 2, R1- and I-clade. LINES can be classified into two subtypes. Subtype 2 has two ORFs: the second (ORF2) encodes a modular protein consisting of an N-terminal apurine/apyrimidine endonuclease domain (EN), a central reverse transcriptase, and a zinc-finger-like domain at the C-terminus. Most non-LTR retrotransposons are inserted throughout the host genome; however, many retrotransposons of the R1 clade exhibit target-specific retrotransposition. This family includes the endonucleases of SART1 and R1bm, from the silkworm Bombyx mori, which belong to the R1-clade. It also includes the endonuclease of snail (Biomphalaria glabrata) Nimbus/Bgl and mosquito Aedes aegypti (MosquI), both which belong to the I-clade. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197311 [Multi-domain]  Cd Length: 205  Bit Score: 43.05  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370   7 WNVNGLRA--CLgkgFLEYVKESDVDIFCIQEskcqegqvelelpgyhQYWNYAEKKGY----SGTAMftkeepIAVTYG 80
Cdd:cd09077     6 INLNRCKAaqDL---LLQTAREEGADIALIQE----------------PYLVPVNNPNWvtdeSGRAA------IVVSDR 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370  81 LG---IEEHDHEGRVITAEFPEYYVVTCYTPNSQDglkrldyrmqwEDAFRAYLKELETK-----KPVIFCGDLNVAHQE 152
Cdd:cd09077    61 LPrkpIQRLSLGLGIVAARVGGITVVSCYAPPSES-----------LEEFEEYLENLVRIvrglsRPVIIGGDFNAWSPA 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 153 IDlkNPKTNRKN---AGFSDEERAkftELLEAGFVDTFRyfypdQEGIYSWwsyrfsaraknagwrIDYFCVSESLKDRL 229
Cdd:cd09077   130 WG--SKRTDRRGrllEDWIANLGL---VLLNDGNSPTFV-----RPRGTSI---------------IDVTFCSPSLARRI 184

                         250       260
                  ....*....|....*....|.
gi 1466031370 230 VDAKIHTEVMGSDHCPVELDI 250
Cdd:cd09077   185 SNWRVLEDETLSDHRYIRFTI 205
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 100-250 1.00e-04

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 42.71  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 100 YYVVTCYTPNSQDGLKRLDYRMQWEDAFRAYLKELETKK--PVIFCGDLNVahqeidlknpktnrkNAGFSDEERAKFTE 177
Cdd:cd09078   128 YHVFGTHLQASDGSCLDRAVRQKQLDELRAFIEEKNIPDnePVIIAGDFNV---------------DKRSSRDEYDDMLE 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 178 LLEAGFVDTFRYF----YPDQEGIYSWWSYRFSaraKNAGWRIDY-FCVSESL-----KDRLVDAKIHTEVMG------- 240
Cdd:cd09078   193 QLHDYNAPEPITAgetpLTWDPGTNLLAKYNYP---GGGGERLDYiLYSNDHLqpsswSNEVEVPKSPTWSVTngytfad 269

                         170
                  ....*....|.
gi 1466031370 241 -SDHCPVELDI 250
Cdd:cd09078   270 lSDHYPVSATF 280
EEP-1 cd09083
Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of ...
 128-250 6.63e-04

Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1; This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.


Pssm-ID: 197317 [Multi-domain]  Cd Length: 252  Bit Score: 39.89  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 128 RAYLKELETKKPVIFCGDLNvahqeidlknpktnrknagfSDEERAKFTELLEAGFVDTFR-YFYPDQEGIYSWWSYRFS 206
Cdd:cd09083   151 LERIKEIAGDLPVILTGDFN--------------------AEPDSEPYKTLTSGGLKDARDtAATTDGGPEGTFHGFKGP 210

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1466031370 207 ARAKnagwRIDYFCVSESLKdrLVDAKIHTEVMG----SDHCPVELDI 250
Cdd:cd09083   211 PGGS----RIDYIFVSPGVK--VLSYEILTDRYDgrypSDHFPVVADL 252
COG2374 COG2374
Predicted extracellular nuclease [General function prediction only];
128-251 7.46e-03

Predicted extracellular nuclease [General function prediction only];


Pssm-ID: 441941 [Multi-domain]  Cd Length: 362  Bit Score: 36.92  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1466031370 128 RAYLKELETKKP---VIFCGDLNvahqeidlknpktnrknagfSDEERAKFTELLEA-GFVDTFRYFYPDQEgiyswWSY 203
Cdd:COG2374   241 RAFVDSLLAADPdapVIVLGDFN--------------------DYPFEDPLRALLGAgGLTNLAEKLPAAER-----YSY 295

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1466031370 204 RFSARAKnagwRIDYFCVSESLKDRLVDAKI-HTEVM-------------------GSDHCPVELDIQ 251
Cdd:COG2374   296 VYDGNSG----LLDHILVSPALAARVTGADIwHINADiynddfkpdfrtyaddpgrASDHDPVVVGLR 359
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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